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Effect of sodium bicarbonate on gel properties and protein conformation of phosphorus-free chicken meat batters
⁎Corresponding author at: School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China.
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Received: ,
Accepted: ,
This article was originally published by Elsevier and was migrated to Scientific Scholar after the change of Publisher.
Abstract
So as to investigate the effect of using sodium bicarbonate (SB) to replace sodium tripolyphosphate (ST) in the chicken meat batters with ST or SB (0.30% and 0.50%), the changes of gel properties and protein conformation were studied. The pH, salt-soluble protein solubility, cooking yield, b* value and texture properties were increased significantly (p < 0.05), the L* and a* values were decreased significantly (p < 0.05) when used the SB to replace ST. The β-sheet structure content was increased, accompanied by the random coil content was decreased (p < 0.05) when used the SB to replace ST. Meanwhile, more hydrophobic interactions were formed and more aliphatic residues were exposed to hydrophilic environment. The secondary and tertiary structures had little affect with the ST or SB were increased from 0.30% to 0.50%. Overall, it was obtained that the use of SB could produce the phosphorus-free chicken meat batters.
Keywords
Sodium tripolyphosphate
Sodium bicarbonate
Salt-soluble protein
Protein conformation
Texture
1 Introduction
In recent years, consumers pay more and more attention to healthy meat products. For their convenience and nutritional values, emulsified meat products are popular all over the word. But most of them added phosphates as phosphates are cheap, effective and easily handled, and supplied some advantages such as increased cooking yield, enhanced texture properties and prolonged the shelf-life, through increased pH, ionic strength, chelate metal ions, salt-soluble protein concentration and induced more protein structure changes (Sarjit and Dykes, 2015; Thangavelu et al., 2019; Gabriel et al., 2020). Some researchers found that phosphorus additives could cause hyperphosphatemia as they have highly bioavailable (almost 100%). It is well known that excessive dietary phosphorus intake can influence the optimal proportion of calcium and phosphorus in human body, which causes bone, cardiovas and cularchronic kidney disease (Yamada et al., 2018; Calvo et al., 2019). However, total or partial removed phosphates were lowered the water holding capacity, texture characteristics and shelf-life. Therefore, it is a challenge to remove them or reduce their amount without any negative effect in the emulsified meat products.
Sodium bicarbonate (SB) is a cheap, convenience and easy soluble in water, which has been widely used in meat products and sea foods to improve water holding capacity, juiciness, texture properties and flavor, as it has stronger buffering capacity and ionic strength (Petracci et al., 2013; Xiong et al., 2020). Zou et al. (2019) showed that the treatment of ultrasound combined with 0.2 M SB promoted the actomyosin of chicken breast meat degeneration, increased in α-helix content and decreased in fluorescence intensity of tyrosine and tryptophan, and increased the MFI, cooking yield and tenderness of cured chicken breast. Xiong et al. (2020) found that the use of SB or ultrasound combined with SB assisted curing could decrease significantly the cooking loss, shear force and surface hydrophobicity of chicken breast meat. Zhu et al. (2018) reported that the chicken meat batter with 0.5% SB had higher pH, cooking yield, textural properties, and β-sheet structure than the sodium chloride. Petracci et al. (2013) stated that as a superior marinating agent, the greater marination performances of SB was used the concentration less than 0.3% in chicken breast meat. For all we know, there is little information about the different changes of gel properties and protein conformation on the application of phosphates and SB in emulsified meat products. Due to sodium tripolyphosphate (ST) is the most popular form of phosphates used in meat industry (Thangavelu et al., 2019), therefore, the aim of this paper was to study the influences on gel properties and protein conformation of chicken batters was made with various amount of ST or SB alone, analyze the possibility of application in chicken meat batters.
2 Material and method
2.1 Materials
The Arbor Acres chickens breast meat was obtained after slaughter 10 min, and was chilled at 2 ± 2 °C for 12 h (pH, 5.90 ± 0.01) in the airtight plastic bags (PE). Then, the meat was ground by the MM-12 grinder (6 mm diameter holes plate, China). About 1.0 kg ground meat was vacuum packaged in nylon/PE bags and frozen storage (−20 °C) less than 14 d. SB and ST were the analytically pure.
2.2 Raw batter preparation
The raw batter was processed according to the method of Zhu et al. (2018). The formulas of raw batters were as follows: chicken breast meat 500 g, water 100 g, ST 1.8 g (T1) or 3 g (T2) alone, or SB 1.8 g (T3) or 3 g (T4) alone.
2.3 pH determined
10 g of raw chicken batter was homogenized at 15,000 rpm for 10 s with 40 mL of distilled water (4 °C) by a homogenizer (T25 digital polytron, IKA Ltd, Germany). After that, the pH was measured immediately (Hanna, Italy).
2.4 Salt-soluble protein (SSP)
The method of SSP of raw chicken batters was according to the procedure of Cofrades et al. (2008).
2.5 Cooking yield
After stored at 2 ± 2 °C overnight, the exudate separated of cooked batter was cleaned and weighed. Applied the following formula to calculate the cooking yield:
Cooking yield% = Weight of cooked batter/Weight of raw batter × 100%.
2.6 Color
The internal color of cooked batter was determined through a CR-400 chromameter (Minolta Camera Co., Japan). The fresh samples with various amount of ST or SB were determined within 1 min.
2.7 Texture measured
The texture profile analysis of cooked batter was measured according to the method of Zhu et al. (2018). The values of hardness (N), springiness, adhesiveness and chewiness (N.mm) were obtained.
2.8 Raman spectroscopic
According to the method of Zhu et al. (2018), the changes of Raman spectroscopic in cooked batters with various amount of ST or SB were measured. The secondary structures were measured according to the amide I and III (Alix et al., 1988), the tertiary structures were measured from the Raman bands centered at 760 cm−1, 830 cm−1 and 850 cm−1 (Herrero et al., 2008). All treatments were measured in four times.
2.9 Statistical analysis
The data was analyzed by an anlysis of variance (ANOVA) and the LSD procedure when significant differences (p < 0.05) were found (SPSS v.18.0).
3 Result and discussion
3.1 pH
Compared to the chicken batters with ST, the pH of the batters with SB were significantly increased (p < 0.05) (Table 1). At the same additive quantity, the pH of the batters with SB were increased about 0.13 units than that of ST. With the ST or SB increased, the pH was significantly increased (p < 0.05). It is well known that ST and SB are acid salt, and easily accept and donate protons, therefore, they have a good buffering capacity and can shift the pH of meat and meat products. In this study, the SB showed a stronger alkaline power in the chicken meat batters than ST, so the batters with SB had a higher pH. The result was agreement with Sheard and Tali (2004), who reported that the pH of pork meat were increased about 0.30 and 0.46 units when added the same concentration of ST or SB alone, respectively. Petracci et al. (2012) also found that the pH of marinaded broiler breast meat were increased 0.3 and 0.7 units when added the same concentration of ST or SB, respectively. Zhu et al. (2018) showed that the pH of chicken batter with 0.5% SB was higher approximately 0.4 units than that of adding sodium chloride. A similar finding manifesting that the pre- and post-chill broiler breast meat were marinated with 3% tetrasodium pyrophosphate or SB in 2% NaCl for 24 h at 4 °C, the pH of breasts with SB were higher than that of tetrasodium pyrophosphate (Sen et al., 2005). T1: 0.3% sodium tripolyphosphate; T2: 0.5% sodium tripolyphosphate; T3: 0.3% sodium bicarbonate; T4: 0.5% sodium bicarbonate. Each value represents the mean ± SD, n = 4. a-dDifferent parameter superscripts in the table indicate significant differences (p < 0.05).
Sample
pH
SSP
L* value
a* value
b* value
T1
6.12 ± 0.02d
18.95 ± 0.95d
83.26 ± 1.06a
2.47 ± 0.14a
11.62 ± 0.18c
T2
6.19 ± 0.03c
21.52 ± 0.87c
82.75 ± 0.96a
2.52 ± 0.12a
11.37 ± 0.20c
T3
6.26 ± 0.02b
23.68 ± 0.82b
80.42 ± 1.27b
1.75 ± 0.18b
12.07 ± 0.19b
T4
6.32 ± 0.04a
25.37 ± 0.76a
80.19 ± 1.35b
1.84 ± 0.15b
13.39 ± 0.15a
3.2 Protein solubility
The changes of SSP concentrations for raw batters with various amounts of ST and SB were effected significantly (Table 1). The SSP concentrations of batters with SB were higher (p < 0.05) than the ST. Increased the ST or SB, the SSP concentrations were significantly increased (p < 0.05). It is well known that pH plays a key role for swelling and dissolving the myofibrillar proteins, because the myofibrillar proteins is improving when the pH is keep away from the isoelectric point (Lee et al., 2015). Kaewjumpol et al. (2013) found that both SB and phosphate could shift the isoelectric point and improve pH, that results in enhancing the SSP extraction. Besides the pH, the ionic strength of meat batter was another important factor to SSP concentrations. Generally, SB can completely dissociate into ions, therefore the batters with SB contained many ions. The use of pyrophosphate alone in chicken red and white muscles has a relatively small effect on ionic strength, and a strong synergistic effect was generated after the addition of sodium chloride. Some researchers reported that because bicarbonates have a higher ionic strength and buffering capacity, they could product a greater effect than the phosphates (Sen et al., 2005).
3.3 Cooking yield
Currently, the cooking yield is used to represent the water holding capacity and quality of raw batter. The cooking yield of the batters with various amount of ST or SB is shown in Fig. 1. Compared to the chicken batters with ST, the cooking yield of the batters with SB were higher (p < 0.05). The main reason is that the batters with SB had a higher pH and SSP concentrations than the ST. SSP, myosin and actin as the main component, which could form gel during heating. More SSP were dissolved and hydration of SSP were generated at higher pH, then more stable gel was formed and lowered the cooking loss (Xiong et al., 2012; Kang et al., 2014; Zhao et al., 2020). Some researchers have reported that the ability to bind and retain water of myofibrillar protein was increased when the pH was increased (Ni et al., 2014; Shen et al., 2019). Kaewthong and Wattanachant (2018) found that compared to the sodium chloride solution, ST and SB had greater capacities to increase the total yield of marinated broiler breast meat at the same electrical conductivity. In the present study, the cooking yield was significantly increased (p < 0.05) with the ST was increased. The reason is possible that the pH and SSP concentrations were increased with increasing ST (Table 1). Meanwhile, with increasing SB, the cooking yield was not significant differences (p > 0.05). The reason is that too much SB added, more carbon dioxide was generated, the gas caused some air holes was formed in the batter and declined the cooking yield (Zhu et al., 2018).
The cooking yield (%) of the chicken batters were made with various amount of sodium tripolyphosphate or sodium bicarbonate. T1: 0.3% sodium tripolyphosphate; T2: 0.5% sodium tripolyphosphate; T3: 0.3% sodium bicarbonate; T4: 0.5% sodium bicarbonate. Each value represents the mean ± SD, n = 4. a-cDifferent parameter superscripts in the figure indicate significant differences (p < 0.05).
3.4 Color
The color of the cooked batters with various amount of ST or SB is presented in Table 1. Compared to the chicken batters with ST, the L* and a* values of the batters with SB were decreased significantly (p < 0.05), to the contrary, the b* value was improved significantly (p < 0.05). The L*, a* and b* values were not affected (p > 0.05) with ST increased. Meanwhile, the L* and a* values were not significant differences (p > 0.05) with ST increased, and b* value was increased significantly (p < 0.05) with increasing SB. The differences in color was possible caused by the differences of function between ST and SB, and the pH and SSP concentration in the batters (Table 1). Increased the pH of meat could enhance the thermal stability of myoglobin, and decrease the denaturation during cooking, therefore increased pinkness (Trout, 1989; Sen et al., 2005). Sen et al. (2005) found that compared to the cooked pre- and post-chill broiler breast meat were marinated with 3% tetrasodium pyrophosphate, the L* values of the SB were increased, b* values were decreased, but the a* values were increased in the pre-chill meat, and not affected in the post-chill meat. Asli and Mørkøre (2012) showed that due to the higher muscle pH, the L* values of salted Atlantic cod with SB had a tendency of decline. In the ground meat products, the L* value was not significant differences (p > 0.05) when the SB or sodium chloride was added (Mohan et al., 2016; Zhu et al., 2018). The differences were produced by the different types of meat products (emulsion and cured meat products). The other, the addition of ST or SB improved the susceptibility of myoglobin during heat denaturation. Thus, the SB had a stronger effect on enhancing the susceptibility of myoglobin in the chicken meat batters than that of ST.
3.5 Texture properties
The texture parameters of cooked chicken batters were effected by the various amount of ST or SB is shown in Table 2. Compared to the chicken batters with ST, the hardness, springiness, adhesiveness, and chewiness of the batters with SB were increased significantly (p < 0.05), and the hardness, springiness, adhesiveness, and chewiness were increased significantly (p < 0.05) with the ST or SB increased. Replaced the ST by SB, and increased the ST or SB, they all improved the ionic strength and pH, increased SSP concentration (Table 1). SSP determines the textural properties of cooked batters, increased SSP concentration could enhance the protein-protein, protein-water and protein-fat interactions, and induce more myosin and actin unfolding, which promoted to form good three-dimensional gels after heating (Zhang et al., 2018; Zheng et al., 2019). The other, higher SSP concentrations promoted more larger size protein aggregations were formed, which induced the gel matrix was more stable and elastic (Kang et al., 2018). Moreover, some researchers reported that the SB increased protein solubility, turbidity of soluble fraction and reactive SH groups, and weaken actomyosin interaction and hydrogen bonds (Chantarasuwan et al., 2011; Saleem et al., 2015). But a relatively small effect on ionic strength was produced in chicken muscles when used pyrophosphate alone, which in combination with sodium chloride can increase ionic strength and as a consequence the solubility of muscular proteins improved (Petracci et al., 2013). Thus, the cooked batters with SB had a better texture than that of ST. T1: 0.3% sodium tripolyphosphate; T2: 0.5% sodium tripolyphosphate; T3: 0.3% sodium bicarbonate; T4: 0.5% sodium bicarbonate. Each value represents the mean ± SD, n = 4. a-dDifferent parameter superscripts in the figure indicate significant differences (p < 0.05).
Sample
Hardness (N)
Springiness
Adhesiveness
Chewiness (N.mm)
T1
37.82 ± 1.22d
0.702 ± 0.012d
0.523 ± 0.011d
18.09 ± 0.52d
T2
42.35 ± 0.96c
0.835 ± 0.015c
0.618 ± 0.009c
21.86 ± 0.48c
T3
47.60 ± 1.05b
0.856 ± 0.013b
0.651 ± 0.014b
27.03 ± 0.56b
T4
51.26 ± 0.81a
0.873 ± 0.016a
0.681 ± 0.012a
31.28 ± 0.61a
3.6 Raman spectroscopic analysis
ST and SB are alkaline, which have an influence on protein structure and break the bonds between proteins. The protein conformation is a key role to research the properties of meat proteins, such as β-sheet structure, Tryptophan and Tyrosine residues (Alix et al., 1988; Li-Chan, 1996). A typical Raman spectroscopic of cooked batters with various amount of ST or SB in the 700–1800 cm−1 is presented in Fig. 2. Table 3 and 4 show the quantitative analysis of the selected peaks from Raman bands, respectively, which indicated with numbers in the Fig. 2. T1: 0.3% sodium tripolyphosphate; T2: 0.5% sodium tripolyphosphate; T3: 0.3% sodium bicarbonate; T4: 0.5% sodium bicarbonate. Each value represents the mean ± SD, n = 4. a-bDifferent parameter superscripts in the figure indicate significant differences (p < 0.05). T1: 0.3% sodium tripolyphosphate; T2: 0.5% sodium tripolyphosphate; T3: 0.3% sodium bicarbonate; T4: 0.5% sodium bicarbonate. Each value represents the mean ± SD, n = 4. a-bDifferent parameter superscripts in the figure indicate significant differences (p < 0.05).
Raman spectra of cooked chicken meat batters were made with various amount of sodium tripolyphosphate or sodium bicarbonate in the region 700–1800 cm−1. T1: 0.3% sodium tripolyphosphate; T2: 0.5% sodium tripolyphosphate; T3: 0.3% sodium bicarbonate; T4: 0.5% sodium bicarbonate.
Sample
α-helice
β-sheet
β-turn
Random coil
T1
50.51 ± 2.23a
21.98 ± 1.45b
16.53 ± 0.53a
11.43 ± 0.25a
T2
49.35 ± 2.12a
22.03 ± 1.37b
16.64 ± 0.48a
11.62 ± 0.17a
T3
47.83 ± 1.96a
25.82 ± 1.42a
16.23 ± 0.42a
10.58 ± 0.21b
T4
47.33 ± 2.26a
25.50 ± 1.50a
16.43 ± 0.51a
10.75 ± 0.19b
Sample
I760/I1003
I850/I830
T1
0.38 ± 0.02a
1.23 ± 0.03b
T2
0.35 ± 0.01a
1.26 ± 0.01b
T3
0.30 ± 0.03b
1.32 ± 0.02a
T4
0.28 ± 0.02b
1.37 ± 0.03a
3.6.1 Secondary structure
The amide I vibrational mode of Raman spectra of cooked batters locates at the intense band about 1660 cm−1, which can supply the information about protein secondary structural, such as C—N stretching, C⚌O stretching and to lesser degrees of peptide groups (Li-Chan, 1996). The overlapping band of 1650–1660 cm−1, 1665–1680 cm−1, 1680 cm−1 and 1660–1665 cm−1 ranges are on behalf of α-helix, β-sheet, β-turn and random coil structures, respectively (Kang et al., 2017). The protein secondary structural were instability when the changes in the hydrogen bonding scheme referring the peptide linkages (Nunes et al., 2019). According to the Fig. 2, the amide I bands of cooked batters with 0.30% and 0.50% ST centered at 1660 ± 0.35 cm−1 and 1660 ± 0.46 cm−1, respectively. When the 0.30% and 0.50% SB were added, the intensity maximum of amide I bands were slightly shift to 1661 ± 0.58 cm−1 and 1661 ± 0.58 cm−1, respectively. The results meant that the improve of β-sheet content together with the decline of α-helix content (Ngarize et al., 2004).
The band of amide III is range from 1225 to 1350 cm−1, which also supplies the information of secondary structural (Li-Chan, 1996; Herrero et al., 2008). A weak band locates range from 1260 to 1300 cm−1 indicates the proteins with higher α-helix structure, a more intense band locates range from 1230 to 1245 cm−1 indicates the β-sheet structure produced, and the band centers near 1245 cm−1 on behalf of the random coil structure form (Herrero et al., 2008). According to the Fig. 2, the amide III bands of cooked batters with 0.30% and 0.50% ST centered at 1268 ± 0.58 cm−1 and 1269 ± 0.83 cm−1, and a weaker peak at 1242 ± 0.58 cm−1 and 1242 ± 0.58 cm−1, respectively. Meanwhile, the peak of cooked batters with 0.30% and 0.50% SB was centered at 1274 ± 0.66 cm−1 and 1275 ± 0.58 cm−1, and a weaker peak at 1237 ± 0.58 cm−1 and 1238 ± 1 cm−1, respectively. These implied that added SB could increase the β-sheet structure content and lower the random coil structure content.
As we can see from the Table 3, compared to the batters with ST, there were significant effected the β-sheet and random coil structure contents in cooked batters with SB. A significant decrease in random coil structure and accompanied by a significant increase (p < 0.05) in β-sheet structure when the addition of SB. Added various amount of ST or SB have not effect (p > 0.05) on secondary structural, respectively. The possible reason is that the pH and ionic strength of raw batters with SB were higher than the ST, which induced more buried residues in protein molecules were exposed, more hydrogen bonds were formed, and protein molecules become more order, then more β-sheet structures were produced during the processing. Some researchers reported that the hardness of gel is enhancing with the β-sheet structure increasing, the result was agreement with the changes of hardness (Table 2) (Zhu et al., 2018). Thus, the use of SB could produce a greater effect on secondary structural than that of ST.
3.6.2 Tertiary structure
The information on the tertiary structure could been supplied by the bands of Raman spectra, such as 760 cm−1, 830 cm−1 and 850 cm−1, which involves mainly about hydrophobic interactions of tryptophan residues and tyrosine residues (Zhu et al., 2018).
The Raman band is centered near 760 cm−1 could provide the information about the stretching vibration of the tryptophan residues ring (Herrero et al., 2008). It was a significant difference (p < 0.05) in the normalized intensities of the 760 cm−1 among the cooked chicken meat batters were made with various amount of ST or SB (Table 4). Compared to the batters with ST, the Raman band locates at 760 cm−1 of the cooked batters with 0.30% and 0.50% SB was significantly decreased (p < 0.05) to 0.30 ± 0.03 and 0.28 ± 0.02, respectively. In addition, there was not significant differences (p > 0.05) in the 760 cm−1 with the ST or SB increased. The results manifested that the SB caused more hydrophobic microenvironment exposure to the polar aqueous solvent than the ST (Herrero et al., 2008; Kang et al., 2017).
The double Raman bands are appointed to vibrations of the para-substituted benzene ring about tyrosine residues, they centered at between 830 cm−1 and 850 cm−1, respectively (Herrero et al., 2008). The I850/I830 could provide the information about exposed or buried in the solvent of the microenvironment around tyrosyl residues. When I850/I830 is the range 0.7 to 1.0, that indicated that the tyrosine residues are buried. On the contrary, when I850/I830 is the range 0.90 to 2.5, that meant the tyrosine residues are exposed to the hydrophilic environment (Li-Chan, 1996). It was a significant difference (p < 0.05) in the I850/I830 among the cooked chicken batters were made with various amount of ST or SB (Table 4). Compared to the batters with ST, the I850/I830 of the cooked batters with 0.30% and 0.50% SB was significantly increased (p < 0.05) to 1.32 ± 0.02 and 1.37 ± 0.03, respectively. In addition, there was not significant differences (p > 0.05) in the I850/I830 with the ST or SB increased. All the I850/I830 of cooked chicken batters were larger than 1.0, which manifested that the ST and SB could induce more tyrosine residues became exposed to hydrophilic environment. In addition, there was not significant differences (p > 0.05) in the I850/I830 with the ST or SB was increased. Overall, due to SB induced more protein denaturation than that of ST, it could promote the tyrosine residues to expose the hydrophilic environment.
4 Conclusion
In the study, the addition of 0.30% and 0.50% ST or SB were significantly effected the gel properties and protein conformation of chicken breast meat batters. The batters with SB have a higher pH, SSP concentrations, cooking yield, b* value and texture properties. Meanwhile, more β-sheet structure and hydrophobic interactions were formed than that of SB. On the contrary, the L* and a* values, random coil structure content and I760/I1003 were decreased significantly. Increased the ST or SB, pH, SSP concentrations, hardness, springiness, adhesiveness, and chewiness were significantly increased, and the color and protein conformation had little affect. From the above, the use of SB could produce the chicken meat batter with higher cooking yield and a stronger gel network.
Acknowledgements
We thanks the Henan province key young teachers training program (no. 2018GGJS114).
Declaration of Competing Interest
The authors (Fei Lu, Zhuang-Li Kang, Li-Peng Wei, Yan-ping Li) declare that there are no financial interests or personal relationships that will influence the work reported in this paper.
References
- Determination of the quantitative secondary structure of proteins by using some parameters of the Raman amide I band. J. Mol. Struct.. 1988;174:159-164.
- [Google Scholar]
- Brines added sodium bicarbonate improve liquid retention and sensory attributes of lightly salted Atlantic cod. LWT - Food Sci. Technol.. 2012;46:196-202.
- [Google Scholar]
- Dietary Phosphate and the Forgotten Kidney Patient: A Critical Need for FDA Regulatory Action. Am. J. Kidney Dis.. 2019;73(4):542-551.
- [Google Scholar]
- The effects of sodium bicarbonate on conformational changes of natural actomyosin from Pacific white shrimp (Litopenaeus vannamei) Food Chem.. 2011;129(4):1636-1643.
- [Google Scholar]
- Characteristics of meat batters with added native and preheated defatted walnut. Food Chem.. 2008;107:1506-1514.
- [Google Scholar]
- Effects of different fish sizes, temperatures and concentration levels of sodium bicarbonate on anaesthesia in Mozambique tilapia (Oreochromis mossambicus) Aquaculture. 2020;529:735716
- [Google Scholar]
- Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment. Food Res. Int.. 2008;41:765-772.
- [Google Scholar]
- Optimizing the electrical conductivity of marinade solution for water-holding capacity of broiler breast meat. Poult. Sci.. 2018;97(2):701-708.
- [Google Scholar]
- Effects of Bicarbonate, Xanthan Gum, and Preparation Methods on Biochemical, Physicochemical, and Gel Properties of Nile Tilapia (Oreochomis niloticus Linn) Mince. J. Aquat. Food Prod. Technol.. 2013;22(3):241-257.
- [Google Scholar]
- Effect of a beating process, as a means of reducing salt content in Chinese-style meatballs (kung-wan): A physical-chemical and textural study. Meat Sci.. 2014;96:147-152.
- [Google Scholar]
- Effect of sodium chloride and processing methods on protein aggregation, physical-chemical and rheological properties of pork batters. Int. J. Food Eng.. 2018;14:5-6.
- [Google Scholar]
- Structural changes evaluation with Raman spectroscopy in meat batters prepared by different processes. J. Food Sci. Technol.-Mysore. 2017;54(9):2852-2860.
- [Google Scholar]
- Functional properties of bicarbonates and lactic acid on chicken breast retail display properties and cooked meat quality. Poult. Sci.. 2015;94(2):302-310.
- [Google Scholar]
- The applications of Raman spectroscopy in food science. Trends Food Sci. Technol.. 1996;7:361-370.
- [Google Scholar]
- Functional properties of bicarbonates on physicochemical attributes of ground beef. LWT - Food Sci. Technol.. 2016;70:333-341.
- [Google Scholar]
- Comparison of changes in the secondary structure of unheated, heated and high-pressure treated blactoglobulin and ovalbumin proteins using Fourier Transform Raman spectroscopy and self deconvolution. J. Agric. Food. Chem.. 2004;52:6470-6477.
- [Google Scholar]
- Gel properties and molecular forces of lamb myofibrillar protein during heat induction at different pH values. Process Biochem.. 2014;49:631-636.
- [Google Scholar]
- Raman spectroscopy and discriminant analysis applied to the detection of frauds in bovine meat by the addition of salts and carrageenan. Microchem. J.. 2019;147:582-589.
- [Google Scholar]
- The use of sodium bicarbonate for marination of broiler breast meat. Poult. Sci.. 2012;9:526-534.
- [Google Scholar]
- Chicken Breast Meat Marinated with Increasing Levels of Sodium Bicarbonate. J. Poultry Sci.. 2013;51(2):206-212.
- [Google Scholar]
- Changes in some biochemical indices of stability of broiler chicken actomyosin at different levels of sodium bicarbonate in presence and absence of sodium chloride. Int. J. Food Prop.. 2015;18(6):1373-1384.
- [Google Scholar]
- Trisodium phosphate and sodium hypochlorite are more effective as antimicrobials against Campylobacter and Salmonella on duck as compared to chicken meat. Int. J. Food Microbiol.. 2015;203:63-69.
- [Google Scholar]
- Effect of chilling, polyphosphate and bicarbonate on quality characteristics of broiler breast meat. Br. Poult. Sci.. 2005;46(4):451-456.
- [Google Scholar]
- Injection of salt, tripolyphosphate and bicarbonate marinade solutions to improve the yield and tenderness of cooked pork loin. Meat Sci.. 2004;68:305-311.
- [Google Scholar]
- Effect of pH on the interaction of porcine myofibrillar proteins with pyrazine compounds. Food Chem.. 2019;287:93-99.
- [Google Scholar]
- Novel processing technologies and ingredient strategies for the reduction of phosphate additives in processed meat. Trends Food Sci. Technol.. 2019;94:43-53.
- [Google Scholar]
- Variation in myoglobin denaturation and color of cooked beef, pork and turkey meat as influenced by pH, sodium chloride, sodium tripolyphosphate and cooking temperature. J. Food Sci.. 1989;54:536-544.
- [Google Scholar]
- Nonmeat ingredients and additives. In: Hui Y.H., ed. Handbook of meat and meat processing. CRC Press; 2012. p. :573-588.
- [Google Scholar]
- Influence of ultrasound-assisted sodium bicarbonate marination on the curing efficiency of chicken breast meat. Ultrason. Sonochem.. 2020;60:104808
- [Google Scholar]
- PiT-2, a type III sodium-dependent phosphate transporter, protects against vascular calcification in mice with chronic kidney disease fed a high-phosphate diet. Kidney Int.. 2018;94(4):716-727.
- [Google Scholar]
- Effects of nanofiber cellulose on functional properties of heat-induced chicken salt-soluble meat protein gel enhanced with microbial transglutaminase. Food Hydrocolloids. 2018;84:1-8.
- [Google Scholar]
- Influence of lard-based diacylglycerol on the rheological and physicochemical properties of thermally induced pork myofibrillar protein gels at different pH levels. LWT - Food Sci. Technol.. 2020;117:108708
- [Google Scholar]
- Partial substitution of NaCl with chloride salt mixtures: Impact on oxidative characteristics of meat myofibrillar protein and their rheological properties. Food Hydrocolloids. 2019;2:36-42.
- [Google Scholar]
- Effect of sodium chloride or sodium bicarbonate in the chicken batters: A physico-chemical and Raman spectroscopy study. Food Hydrocolloids. 2018;83:222-228.
- [Google Scholar]
- Combined effect of ultrasound and sodium bicarbonate marination on chicken breast tenderness and its molecular mechanism. Ultrason. Sonochem.. 2019;59:104735
- [Google Scholar]
